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MD simulations of Mistic: conformational stability in detergent micelles and water.

Abstract:

Mistic is an unusual membrane protein from Bacillus subtilis. It appears to fold and insert autonomously into a lipid bilayer and has been suggested as a tool that aids the targeting of eukaryotic membrane proteins to bacterial membranes. The NMR structure of Mistic in detergent (LDAO) micelles has revealed it to be a four alpha-helix bundle. From a structural perspective, Mistic does not resemble other membrane proteins. Its external surface is not very hydrophobic, and standard methods do n...

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Publication status:
Published

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Publisher copy:
10.1021/bi0608818

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Journal:
Biochemistry
Volume:
45
Issue:
30
Pages:
9053-9058
Publication date:
2006-08-01
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
Source identifiers:
100674
Language:
English
Keywords:
Pubs id:
pubs:100674
UUID:
uuid:4fa5262e-d58c-4082-8ba2-61ec6cac123e
Local pid:
pubs:100674
Deposit date:
2012-12-19

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